C1CSH7 · DAPB_STRZT

Function

function

Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.

Caution

Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.

Catalytic activity

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site9-14NAD+ (UniProtKB | ChEBI)
Binding site35NAD+ (UniProtKB | ChEBI)
Binding site89-91NAD+ (UniProtKB | ChEBI)
Binding site115-118NAD+ (UniProtKB | ChEBI)
Active site145Proton donor/acceptor
Binding site146(S)-2,3,4,5-tetrahydrodipicolinate (UniProtKB | ChEBI)
Active site149Proton donor
Binding site155-156(S)-2,3,4,5-tetrahydrodipicolinate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function4-hydroxy-tetrahydrodipicolinate reductase
Molecular FunctionNAD binding
Molecular FunctionNADP binding
Molecular Functionoxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
Biological Processdiaminopimelate biosynthetic process
Biological Processlysine biosynthetic process via diaminopimelate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    4-hydroxy-tetrahydrodipicolinate reductase
  • EC number
  • Short names
    HTPA reductase

Gene names

    • Name
      dapB
    • Ordered locus names
      SPT_1497

Organism names

Accessions

  • Primary accession
    C1CSH7

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001897601-2554-hydroxy-tetrahydrodipicolinate reductase

Structure

Family & Domains

Sequence similarities

Belongs to the DapB family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    255
  • Mass (Da)
    27,837
  • Last updated
    2009-05-26 v1
  • Checksum
    BDE4464A11633BC5
MSIRVIIAGFKGKMGQAACQMVLTDPDLDLVAVLDPFESESEWQGIPVFKDKADLAGFEADVWVDFTTPAVAYENTRFALENGFAPVVGTTGFTSEEIAELKEFSRAQDLGGLIAPNFALGAVLLMQFATQAAKYFPNVEIIELHHDKKKDAPSGTAIKTAELMAEVRESIQQGAADEEELIAGARGADFDGMRIHSVRLPGLVAHQEVIFGNQGEGLTLRHDSYDRISFMTGVNLGIKEVVKRHELVYGLEHLL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000921
EMBL· GenBank· DDBJ
ACO24090.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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